J KUSHARI

T CHATTERJEE

M MUKHERJEA

University of Calcutta (informally known as Calcutta University or CU) is a collegiate public state university located in Kolkata, West Bengal, India.&nbsp;Within India it is recognized as a &quot;Five-Star University&quot; and accredited &quot;A&quot; Grade by National Assessment and Accreditation Council.

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The University of Calcutta has secured the Fifth position among the Universities of India in the prestigious &quot;Indian University Ranking 2019&quot; list, released by the NIRF of the Ministry of Human Resource Development, Government of India.

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It was established on 24 January 1857, and was one of the first institutions in Asia to be established as a multidisciplinary and Western-style university. Its alumni and faculty include several heads of state, heads of government, social reformers, prominent artists, only academy award winner and Dirac medal winner in India, many Fellows of the Royal Society and five Nobel laureates as of 2019 which is highest in South Asia.

University Of Calcutta

290. Acid phosphatase activity in developing human placenta

Journal of Steroid Biochemistry

The presence of phosphodiesterase IV has been demonstrated in the human fetal brain, liver and placenta as early as in the 6th week of intrauterine development. The enzyme activity in each tissue increases with gestation, being maximum at 18-21 wk and then decreases. The Km values of this enzyme for bis-(p-nitrophenyl)-phosphate hydrolysis in the brain, liver and placenta are 2.94 mM, 1.47 mM and 1.66 mM, respectively. Presence of sulfhydryl group in the active center of the placental enzyme has been demonstrated with the help of cationic study. EDTA inhibits the enzyme in all the three tissues. Effect of concanavalin A reveals the absence or unexposition of glucose, mannose and N-acetylglucosamine moieties in the active site of the enzyme in each of the three tissues. Maximum enzyme activity has been found to be localized in the soluble supernatant fraction obtained on centrifuging the brain and liver homogenate at 105,000 × g and in 20,000 × g pellet of the placenta. © 1982.

European Journal of Obstetrics and Gynecology and Reproductive Biology

Occurrence of phosphodiesterase IV in the developing human brain, liver and placenta

Subfractional activities and some properties of β-glucuronidase were studied at different ontogenetic stages of the human placenta. Maximum activity was localized in the 105,000g supernatant of tissue homogenatc. The enzyme activity in all fractions increased gradually, being maximum in the placentas of 22-26 weeks of gestation. At term, β-glucuronidase activity had diminished to a great extent. The enzyme showed considerable stability after heating at 65 °C for 10 min. The K<inf>m</inf>value of this enzyme for p-nitrophenyl-β-D-glucuronide was 1.02 mM. EDTA inhibited placental β-glucuronidase. Of the cations tested, Ag+, Fe++and Co++were stimulatory, while Zn++was inhibitory to the enzyme. Only one isoenzyme of β-glucuronidase was found in human placenta. © 1980 S. Karger AG, Basel.

Gynecologic and Obstetric Investigation

Studies on Î²-glucuronidase of the developing human placenta

Mitochondrial lipids and ATPasc activity have been studied in developing human placenta. The enzyme activity in the placenta increases steadily with gestational age until the 18th to 21st week, and decreases in the second half of pregnancy. Both Mg2+ and Ca2+ ions have been found to activate the enzyme system. The solubilization of membrane lipids by deoxycholate inhibits the enzyme activity. Total lipid and total phospholipid contents of the mitochondrial membranes also increase during the early development of the placenta with peaks in the 14th to 17th week, after which the levels decrease. Howevcr, the percentage composition of individual phospholipids remains almost the same throughout pregnancy. The profile of the ATPase activity exhibits a correlation with that of membrane lipids in human placenta during intrauterine development of the tissue. © 1980 S. Karger AG, Basel.

Journal	Journal of Steroid Biochemistry
Publisher	-
ISSN	0022-4731